메뉴 건너뛰기




Volumn 17, Issue 20, 1998, Pages 6096-6105

Polymerization of bacteriophage ∅29 replication protein p1 into protofilament sheets

Author keywords

Membrane associated protein; Protofilament sheets; Viral DNA replication

Indexed keywords

BLOOD CLOTTING FACTOR 10A; HYBRID PROTEIN; MEMBRANE PROTEIN; TUBULIN; VIRUS DNA; CARRIER PROTEIN; MALTOSE BINDING PROTEIN; MALTOSE-BINDING PROTEIN; PHAGE PHI29 PROTEIN P1; POLYMER; VIRUS PROTEIN;

EID: 0032531536     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1093/emboj/17.20.6096     Document Type: Article
Times cited : (25)

References (32)
  • 1
    • 0030612613 scopus 로고    scopus 로고
    • Phage ø29 protein p6 is in a monomer-dimer equilibrium that shifts to higher association states at the millimolar concentrations found in vivo
    • Abril ,A.M., Salas,M., Andreu,J.M., Hermoso,J.M. and Rivas,G. (1997) Phage ø29 protein p6 is in a monomer-dimer equilibrium that shifts to higher association states at the millimolar concentrations found in vivo. Biochemistry, 36, 11901-11908.
    • (1997) Biochemistry , vol.36 , pp. 11901-11908
    • Abril, A.M.1    Salas, M.2    Andreu, J.M.3    Hermoso, J.M.4    Rivas, G.5
  • 2
    • 0031591144 scopus 로고    scopus 로고
    • Initiation of bacteriophage ø29 DNA replication in vivo: Assembly of a membrane-associated multiprotein complex
    • Bravo,A. and Salas,M. (1997) Initiation of bacteriophage ø29 DNA replication in vivo: Assembly of a membrane-associated multiprotein complex. J. Mol. Biol., 269, 102-112.
    • (1997) J. Mol. Biol. , vol.269 , pp. 102-112
    • Bravo, A.1    Salas, M.2
  • 3
    • 0025336602 scopus 로고
    • Functional analysis of the Bacillus subtilis bacteriophage SPP1 pac site
    • Bravo,A., Alonso,J.C. and Trautner,T.A. (1990) Functional analysis of the Bacillus subtilis bacteriophage SPP1 pac site. Nucleic Acids Res., 18, 2881-2886.
    • (1990) Nucleic Acids Res. , vol.18 , pp. 2881-2886
    • Bravo, A.1    Alonso, J.C.2    Trautner, T.A.3
  • 4
    • 0028000275 scopus 로고
    • A genetic approach to the identification of functional amino acids in protein p6 of Bacillus subtilis phage ø29
    • Bravo,A., Hermoso,J.M. and Salas,M. (1994) A genetic approach to the identification of functional amino acids in protein p6 of Bacillus subtilis phage ø29. Mol. Gen. Genet., 245, 529-536.
    • (1994) Mol. Gen. Genet. , vol.245 , pp. 529-536
    • Bravo, A.1    Hermoso, J.M.2    Salas, M.3
  • 5
    • 0344250735 scopus 로고
    • Thermal regulation of membrane lipid fluidity in bacteria
    • de Mendoza,D. and Cronan,J.E.Jr (1983) Thermal regulation of membrane lipid fluidity in bacteria. Trends Biochem. Sci., 8, 49-52.
    • (1983) Trends Biochem. Sci. , vol.8 , pp. 49-52
    • De Mendoza, D.1    Cronan Jr., J.E.2
  • 6
    • 0015957585 scopus 로고
    • Microtubule surface lattice and subunit structure and observations on reassembly
    • Erickson,H.P. (1974) Microtubule surface lattice and subunit structure and observations on reassembly. J. Cell Biol., 60, 153-167.
    • (1974) J. Cell Biol. , vol.60 , pp. 153-167
    • Erickson, H.P.1
  • 7
    • 0028872562 scopus 로고
    • FtsZ, a prokaryotic homolog of tubulin?
    • Erickson,H.P. (1995) FtsZ, a prokaryotic homolog of tubulin? Cell, 80, 367-370.
    • (1995) Cell , vol.80 , pp. 367-370
    • Erickson, H.P.1
  • 8
    • 0030829601 scopus 로고    scopus 로고
    • FtsZ, a tubulin homologue, in prokaryote cell division
    • Erickson, H.P. (1997) FtsZ, a tubulin homologue, in prokaryote cell division, Trends Cell Biol., 7, 362-367.
    • (1997) Trends Cell Biol. , vol.7 , pp. 362-367
    • Erickson, H.P.1
  • 9
    • 0030266954 scopus 로고    scopus 로고
    • Protofilaments and rings, two conformations of the tubulin family conserved from bacterial FtsZ to αβ and γ tubulin
    • Erickson,H.P. and Stoffler.D. (1996) Protofilaments and rings, two conformations of the tubulin family conserved from bacterial FtsZ to αβ and γ tubulin. J. Cell Biol., 135, 5-8.
    • (1996) J. Cell Biol. , vol.135 , pp. 5-8
    • Erickson, H.P.1    Stoffler, D.2
  • 10
    • 0030068218 scopus 로고    scopus 로고
    • Bacterial cell division protein FtsZ assembles into protofilament sheets and minirings, structural homologs of tubulin polymers
    • Erickson,H.P, Taylor,D.W., Taylor,K.A. and Bramhill,D. (1996) Bacterial cell division protein FtsZ assembles into protofilament sheets and minirings, structural homologs of tubulin polymers. Proc. Natl Acad. Sci. USA, 93, 519-523.
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 519-523
    • Erickson, H.P.1    Taylor, D.W.2    Taylor, K.A.3    Bramhill, D.4
  • 11
    • 0017663070 scopus 로고
    • Zinc ion-induced assembly of tubulin
    • Gaskin,F. and Kress,Y. (1977) Zinc ion-induced assembly of tubulin. J. Biol., Chem., 252, 6918-6924.
    • (1977) J. Biol., Chem. , vol.252 , pp. 6918-6924
    • Gaskin, F.1    Kress, Y.2
  • 12
    • 0032053588 scopus 로고    scopus 로고
    • Intermediate filament assembly: Fibrillogenesis is driven by decisive dimer-dimer interactions
    • Herrmann,H. and Aebi,U. (1998) Intermediate filament assembly: fibrillogenesis is driven by decisive dimer-dimer interactions. Curr. Opin. Struct. Biol., 8, 177-185.
    • (1998) Curr. Opin. Struct. Biol. , vol.8 , pp. 177-185
    • Herrmann, H.1    Aebi, U.2
  • 13
    • 0015875908 scopus 로고
    • DNA replication in bacteriophage ø29: The requirement of a viral-specific product for association of ø29 DNA with the cell membrane of Bacillus amyloliquefaciens
    • Ivarie,R.D. and Pe ̀ne,J.J. (1973) DNA replication in bacteriophage ø29: the requirement of a viral-specific product for association of ø29 DNA with the cell membrane of Bacillus amyloliquefaciens. Virology, 52, 351-362.
    • (1973) Virology , vol.52 , pp. 351-362
    • Ivarie, R.D.1    Pegrave2    ne, J.J.3
  • 14
    • 0030271515 scopus 로고    scopus 로고
    • Coiled coils: New structures and new functions
    • Lupas,A. (1996) Coiled coils: new structures and new functions. Trends Biochem. Sci., 21, 375-382.
    • (1996) Trends Biochem. Sci. , vol.21 , pp. 375-382
    • Lupas, A.1
  • 15
    • 0026356891 scopus 로고
    • Predicting coiled-coils from protein sequences
    • Lupas,A., van Dyke,M. and Stock,J. (1991) Predicting coiled-coils from protein sequences. Science, 252, 1162-1164.
    • (1991) Science , vol.252 , pp. 1162-1164
    • Lupas, A.1    Van Dyke, M.2    Stock, J.3
  • 16
    • 0040528887 scopus 로고    scopus 로고
    • Protein-primed DNA replication: A transition between two modes of priming by a unique DNA polymerase
    • Méndez,J., Blanco,L. and Salas,M. (1997) Protein-primed DNA replication: a transition between two modes of priming by a unique DNA polymerase. EMBO J., 16, 2519-2527.
    • (1997) EMBO J. , vol.16 , pp. 2519-2527
    • Méndez, J.1    Blanco, L.2    Salas, M.3
  • 18
    • 0016127731 scopus 로고
    • Suppressorsensitive mutants and genetic map of Bacillus subtilis bacteriophage ø29
    • Moreno,F., Camacho,A., Viñuela,E. and Salas,M. (1974) Suppressorsensitive mutants and genetic map of Bacillus subtilis bacteriophage ø29. Virology, 62, 1-16.
    • (1974) Virology , vol.62 , pp. 1-16
    • Moreno, F.1    Camacho, A.2    Viñuela, E.3    Salas, M.4
  • 19
    • 0019800463 scopus 로고
    • Silver stain for proteins in polyacrylamide gels: A modified procedure with enhanced uniform sensitivity
    • Morrissey,J.H. (1981) Silver stain for proteins in polyacrylamide gels: a modified procedure with enhanced uniform sensitivity. Anal. Biochem., 117, 307-310.
    • (1981) Anal. Biochem. , vol.117 , pp. 307-310
    • Morrissey, J.H.1
  • 20
    • 0032518656 scopus 로고    scopus 로고
    • Dynamic assembly of FtsZ regulated by GTP hydrolysis
    • Mukherjee,A. and Lutkenhaus,J. (1998) Dynamic assembly of FtsZ regulated by GTP hydrolysis. EMBO J., 17, 462-469.
    • (1998) EMBO J. , vol.17 , pp. 462-469
    • Mukherjee, A.1    Lutkenhaus, J.2
  • 21
    • 0024514654 scopus 로고
    • Characterization, overproduction and purification of the product of gene 1 of Bacillus subtilis phage ø29
    • Prieto, I., Mendez,E. and Salas,M. (1989) Characterization, overproduction and purification of the product of gene 1 of Bacillus subtilis phage ø29. Gene, 77, 195-204.
    • (1989) Gene , vol.77 , pp. 195-204
    • Prieto, I.1    Mendez, E.2    Salas, M.3
  • 22
    • 0015875764 scopus 로고
    • Genetic study of suppressor-sensitive mutants of the Bacillus subtilis bacteriophage ø29
    • Reilly, B.E., Zeece,V.M. and Anderson,D.L. (1973) Genetic study of suppressor-sensitive mutants of the Bacillus subtilis bacteriophage ø29. J. Virol., 11, 756-760.
    • (1973) J. Virol. , vol.11 , pp. 756-760
    • Reilly, B.E.1    Zeece, V.M.2    Anderson, D.L.3
  • 23
    • 0030901357 scopus 로고    scopus 로고
    • Bacterial cell division: The cycle of the ring
    • Rothfield,L.I. and Justice,S.S. (1997) Bacterial cell division: The cycle of the ring. Cell, 88, 581-584.
    • (1997) Cell , vol.88 , pp. 581-584
    • Rothfield, L.I.1    Justice, S.S.2
  • 24
    • 0002277375 scopus 로고    scopus 로고
    • Mechanisms for priming DNA synthesis
    • Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • Salas,M., Miller,J.T., Leis,J. and DePamphilis,M.L. (1996) Mechanisms for priming DNA synthesis. In DNA Replication in Eukaryotic Cells. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY, pp. 131-176.
    • (1996) DNA Replication in Eukaryotic Cells , pp. 131-176
    • Salas, M.1    Miller, J.T.2    Leis, J.3    DePamphilis, M.L.4
  • 27
    • 0023472472 scopus 로고
    • Tricine-sodium dodecyl sulfate- Polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa
    • Schagger,H. and Jagow,G. (1987) Tricine-sodium dodecyl sulfate- polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa. Anal. Biochem., 166, 368-379.
    • (1987) Anal. Biochem. , vol.166 , pp. 368-379
    • Schagger, H.1    Jagow, G.2
  • 28
    • 0025034523 scopus 로고
    • The structure of microtubule ends during the elongation and shortening phases of dynamic instability examined by negative-stain electron microscopy
    • Simon,J.R. and Salmon,E.D. (1990) The structure of microtubule ends during the elongation and shortening phases of dynamic instability examined by negative-stain electron microscopy. J. Cell Sci., 96, 571-582.
    • (1990) J. Cell Sci. , vol.96 , pp. 571-582
    • Simon, J.R.1    Salmon, E.D.2
  • 29
    • 0015181809 scopus 로고
    • Temperaturesensitive mutants of bacteriophage ø29
    • Talavera,A., Jiménez,F., Salas,M. and Vinuela,E. (1971) Temperaturesensitive mutants of bacteriophage ø29. Virology, 46, 586-595.
    • (1971) Virology , vol.46 , pp. 586-595
    • Talavera, A.1    Jiménez, F.2    Salas, M.3    Vinuela, E.4
  • 30
    • 0021258393 scopus 로고
    • The kinetics of microtubule assembly. Evidence for a two-stage nucleation mechanism
    • Voter,W.A. and Erickson,H.P. (1984) The kinetics of microtubule assembly. Evidence for a two-stage nucleation mechanism. J. Biol. Chem., 259, 10430-10438.
    • (1984) J. Biol. Chem. , vol.259 , pp. 10430-10438
    • Voter, W.A.1    Erickson, H.P.2
  • 31
    • 0019967769 scopus 로고
    • Nucleotide sequence of the major early region of bacteriophage ø29
    • Yoshikawa,H, and Ito,J. (1982) Nucleotide sequence of the major early region of bacteriophage ø29. Gene, 17, 323-335.
    • (1982) Gene , vol.17 , pp. 323-335
    • Yoshikawa, H.1    Ito, J.2
  • 32
    • 0030815131 scopus 로고    scopus 로고
    • 2+-mediated GTP-dependent dynamic assembly of bacterial cell division protein FtsZ into asters and polymer networks in vitro
    • 2+-mediated GTP-dependent dynamic assembly of bacterial cell division protein FtsZ into asters and polymer networks in vitro. EMBO J., 16, 5455-5463.
    • (1997) EMBO J. , vol.16 , pp. 5455-5463
    • Yu, X.1    Margolin, W.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.